ω-Conotoxin GVIA

ω-Conotoxin GVIA is isolated from the venom of the fish-hunting snail Conus geographus. It has a role as a venom, a neurotoxin, a calcium channel blocker, and a marine metabolite.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
ω-Conotoxin GVIA(CAS 106375-28-4)

CAT No: 10-101-281

CAS No:106375-28-4

Synonyms/Alias:omega-Conotoxin G via;106375-28-4;Omega conopeptide GVIA (Conus);SNX124;SNX-124;SNX 124;Omega-Conotoxin GVIA trifluoroacetate salt;Omega-Conotoxin G Via TFA;PCN-4161-V;DA-59381;Q27162637;H-D-Cys(1)-Lys-Ser-D-aHyp-Gly-D-Ser-D-Ser-Cys(2)-Ser-aHyp-D-aThr-Ser-D-Tyr-Asn-Cys(3)-Cys(1)-Arg-D-Ser-Cys(2)-Asn-D-aHyp-Tyr-aThr-D-Lys-Arg-Cys(3)-Tyr-NH2;

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M.F/Formula
C120H182N38O43S6
M.W/Mr.
3037.4
Sequence
One Letter Code:CKSXGSSCSXXSYNCCRSCNXYXKRCY
Three Letter Code:H-DL-Cys(1)-DL-Lys-DL-Ser-DL-xiHyp-Gly-DL-Ser-DL-Ser-DL-Cys(2)-DL-Ser-DL-xiHyp-DL-xiThr-DL-Ser-DL-Tyr-DL-Asn-DL-Cys(3)-DL-Cys(1)-DL-Arg-DL-Ser-DL-Cys(2)-DL-Asn-DL-xiHyp-DL-Tyr-DL-xiThr-DL-Lys-DL-Arg-DL-Cys(3)-DL-Tyr-NH2
Application
N-type calcium channel blocker

ω-Conotoxin GVIA is a highly specialized peptide toxin originally isolated from the venom of the marine cone snail Conus geographus. Characterized by its unique disulfide-rich structure, ω-Conotoxin GVIA is renowned for its potent and selective inhibition of N-type voltage-gated calcium channels (Cav2.2). This property has established it as an invaluable molecular tool in neurobiological research, enabling precise modulation of synaptic transmission and neuronal excitability. The compound's stability and specificity make it particularly useful for dissecting the roles of calcium channels in various physiological and pathological processes, and its application extends across a broad spectrum of scientific disciplines, from basic neuroscience to advanced pharmacological investigations.

Neuroscience Research: In the field of neuroscience, ω-Conotoxin GVIA is extensively utilized to elucidate the functional roles of N-type calcium channels in neuronal communication. By selectively blocking these channels, researchers can investigate the mechanisms underlying neurotransmitter release, neuronal plasticity, and synaptic modulation. The ability to distinguish N-type channel contributions from other calcium channel subtypes allows for detailed mapping of synaptic pathways and enhances understanding of complex neural circuits. This peptide has become a standard tool in electrophysiological studies, facilitating the exploration of channelopathies and neurophysiological disorders.

Pain Mechanism Studies: As a potent inhibitor of Cav2.2 channels, ω-Conotoxin GVIA plays a pivotal role in pain research, particularly in the investigation of nociceptive pathways. By blocking the influx of calcium ions in presynaptic terminals, it effectively suppresses the release of neurotransmitters involved in pain signal transmission. This mechanism enables scientists to delineate the specific involvement of N-type channels in chronic and acute pain models, providing a foundation for the development of novel analgesic strategies and enhancing the understanding of pain modulation at the molecular level.

Synaptic Transmission Analysis: The application of ω-Conotoxin GVIA extends to the detailed analysis of synaptic transmission in both central and peripheral nervous systems. By selectively inhibiting N-type calcium channels, researchers can isolate and characterize the contributions of these channels to excitatory and inhibitory neurotransmission. This approach is instrumental in studies aiming to unravel the dynamics of synaptic vesicle release, synaptic plasticity, and the regulation of neuronal networks. The use of this peptide enables precise manipulation of synaptic activity, supporting advanced investigations into neurodevelopmental and neurodegenerative processes.

Pharmacological Screening: In drug discovery and pharmacological research, ω-Conotoxin GVIA serves as a critical reference compound for screening and characterizing new modulators of voltage-gated calcium channels. Its high specificity provides a benchmark for evaluating the efficacy and selectivity of novel channel inhibitors or modulators. This application is crucial for identifying candidate molecules with potential therapeutic value and for understanding the pharmacological profiles of experimental compounds targeting neuronal calcium channels.

Ion Channel Functional Studies: Beyond its applications in neuroscience and pharmacology, ω-Conotoxin GVIA is employed in broader ion channel research to probe the biophysical properties and regulatory mechanisms of N-type calcium channels. Researchers utilize it to investigate channel gating, permeability, and modulation by intracellular signaling pathways. The insights gained from these studies contribute to the broader understanding of calcium channel diversity and function in excitable cells, supporting advancements in cellular physiology and molecular neuroscience.

Biochemical Pathway Elucidation: The use of ω-Conotoxin GVIA is integral to the study of intracellular signaling cascades initiated by calcium influx. By selectively inhibiting Cav2.2 channels, scientists can dissect the downstream effects of calcium channel blockade on gene expression, enzyme activation, and second messenger systems. This approach aids in mapping the intricate networks of cellular communication and enhances the understanding of how calcium signaling integrates with other biochemical pathways to regulate cell function and survival.

Long-term Storage Conditions
Soluble to 1 mg/ml in water
Shipping Condition
Shipped at room temperature
InChI
InChI=1S/C120H182N38O43S6/c1-53(165)91-114(197)138-66(10-4-6-26-122)95(178)136-68(12-8-28-132-120(129)130)98(181)149-81(107(190)139-69(93(126)176)29-55-13-19-58(167)20-14-55)49-204-207-52-84-110(193)153-80-48-203-202-47-64(123)94(177)135-65(9-3-5-25-121)97(180)147-78(45-163)117(200)156-38-61(170)32-85(156)111(194)133-37-90(175)134-74(41-159)102(185)145-76(43-161)105(188)152-83(109(192)148-79(46-164)118(201)158-40-63(172)34-87(158)113(196)155-92(54(2)166)115(198)146-77(44-162)103(186)140-70(30-56-15-21-59(168)22-16-56)99(182)141-72(35-88(124)173)100(183)150-84)51-206-205-50-82(151-104(187)75(42-160)144-96(179)67(137-106(80)189)11-7-27-131-119(127)128)108(191)143-73(36-89(125)174)116(199)157-39-62(171)33-86(157)112(195)142-71(101(184)154-91)31-57-17-23-60(169)24-18-57/h13-24,53-54,61-87,91-92,159-172H,3-12,25-52,121-123H2,1-2H3,(H2,124,173)(H2,125,174)(H2,126,176)(H,133,194)(H,134,175)(H,135,177)(H,136,178)(H,137,189)(H,138,197)(H,139,190)(H,140,186)(H,141,182)(H,142,195)(H,143,191)(H,144,179)(H,145,185)(H,146,198)(H,147,180)(H,148,192)(H,149,181)(H,150,183)(H,151,187)(H,152,188)(H,153,193)(H,154,184)(H,155,196)(H4,127,128,131)(H4,129,130,132)
InChI Key
FDQZTPPHJRQRQQ-UHFFFAOYSA-N
Canonical SMILES
CC(C1C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2CSSCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C3CC(CN3C(=O)C(NC(=O)C4CSSCC(C(=O)NC(C(=O)N5CC(CC5C(=O)N1)O)CO)NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C6CC(CN6C(=O)C(NC(=O)C(NC(=O)C(CSSCC(C(=O)NC(C(=O)NC(C(=O)N4)CO)CCCNC(=N)N)NC2=O)N)CCCCN)CO)O)CO)CO)CC(=O)N)O)CC7=CC=C(C=C7)O)C(C)O)CCCCN)CCCNC(=N)N)C(=O)NC(CC8=CC=C(C=C8)O)C(=O)N)CC(=O)N)CC9=CC=C(C=C9)O)CO)O
Isomeric SMILES
C[C@H]([C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H]2CSSC[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H]3C[C@H](CN3C(=O)[C@@H](NC(=O)[C@@H]4CSSC[C@@H](C(=O)N[C@H](C(=O)N5C[C@@H](C[C@H]5C(=O)N1)O)CO)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)[C@@H]6C[C@H](CN6C(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N4)CO)CCCNC(=N)N)NC2=O)N)CCCCN)CO)O)CO)CO)CC(=O)N)O)CC7=CC=C(C=C7)O)[C@@H](C)O)CCCCN)CCCNC(=N)N)C(=O)N[C@@H](CC8=CC=C(C=C8)O)C(=O)N)CC(=O)N)CC9=CC=C(C=C9)O)CO)O

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